Results 201 to 210 of about 95,153 (249)

Comprehensive Peptide Profiling Reveals the Influence of Streptococcus Thermophilus, Lactobacillus Delbrueckii Subsp. bulgaricus, and Endogenous Milk Proteases on the Hydrolysis of Milk Proteins During Early‐Stage Lactic Acid Fermentation

open access: yesChemFoodChem, EarlyView.
Untargeted peptide profiling investigates how S. thermophilus, Lb. bulgaricus, and endogenous milk enzymes impact proteolysis during early‐stage milk fermentation. ≥ 3000 identified peptides show the strongest influence of LB on the peptide profile and number of bioactive peptides. Shorter peptides are mostly formed by LB and hydrolyzed by ST.
Eva Beck   +6 more
wiley   +1 more source

Synthetic Strategies for Activity‐Based Probes to Decode Ubiquitin‐Like Modifiers

open access: yesChemistry – A European Journal, EarlyView.
ABSTRACT Ubiquitin‐like proteins (Ubls) such as SUMO, NEDD8, ISG15, URM1, UFM1, FAT10, ATG8/ATG12, and FUBI are essential regulators of cellular homeostasis, controlling processes from protein stability and trafficking to immune signaling and autophagy.
Saibal Chanda   +5 more
wiley   +1 more source
Some of the next articles are maybe not open access.

Related searches:

An Overview of Serine Proteases

Current Protocols in Protein Science, 2001
AbstractThis unit summarizes the families of serine proteases and their mechanism of catalysis. Methods for assays and determining substrate specificity are briefly described. The mode of action of commonly available inhibitors is also included.
openaire   +2 more sources

Hydrolysis of polyesters by serine proteases

Biotechnology Letters, 2005
The substrate specificity of alpha-chymotrypsin and other serine proteases, trypsin, elastase, proteinase K and subtilisin, towards hydrolysis of various polyesters was examined using poly(L-lactide) (PLA), poly(beta-hydroxybutyrate) (PHB), poly(ethylene succinate) (PES), poly(ethylene adipate) (PEA), poly(butylene succinate) (PBS), poly(butylene ...
Hyun-A, Lim, Takao, Raku, Yutaka, Tokiwa
openaire   +2 more sources

Inhibition of serine proteases by steroids

Biochemical Pharmacology, 1982
Proteolysis of 14C-labeled globin, as well as the hydrolysis of the specific substrate benzoyl tyrosine ethyl ester, by purified bovine chymotrypsin was found to be inhibited by several steroid hormones. The inhibition of chymotrypsin by the steroids was of a competitive nature, with Ki values of 9.9 x 10(-5) M for triamcinolone (9-fluoro-11 beta, 16 ...
M, Mayer, B, Neufeld, Z, Finci
openaire   +2 more sources

Genomic overview of serine proteases

Biochemical and Biophysical Research Communications, 2003
Serine proteases (SP) are peptidases with a uniquely activated serine residue in the substrate-binding pocket. They represent about 0.6% of all proteins in the human genome. SP are involved in many vital functions such as digestion, blood clotting, fibrinolysis, fertilization, and complement activation and are related to many diseases including cancer,
George M, Yousef   +3 more
openaire   +2 more sources

Strategies for the inhibition of serine proteases

Cellular and Molecular Life Sciences, 2001
Serine proteases have been shown to play a multifarious role in health and disease. As a result, there has been considerable interest in the design and development of synthetic inhibitors of these enzymes. In view of their diverse roles in biological processing events, one of the great challenges in such endeavours has been the need to produce ...
B, Walker, J F, Lynas
openaire   +2 more sources

Serine proteases and cardiac function

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2005
The serine proteases of the trypsin superfamily are versatile enzymes involved in a variety of biological processes. In the cardiovascular system, the importance of these enzymes in blood coagulation, platelet activation, fibrinolysis, and thrombosis has been well established.
Qingyu, Wu   +2 more
openaire   +2 more sources

The novel inhibitors of serine proteases

Amino Acids, 2009
Thirty optically active nonprotein alpha-amino acids and peptides based thereon have been screened for their ability to interact with bovine trypsin and proteinase K from Tritirachium album Limber, which belong to the group of serine proteases. Both structure-based drug design approach and determination of enzyme activity have been used to identify low
N, Hovhannisyan   +7 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy